PURIFICATION OF GLUTATHIONE-REDUCTASE FROM PORCINE ERYTHROCYTES BY THE USE OF AFFINITY CHROMATOGRAPHY ON 2',5'-ADP-SEPHAROSE 4B AND CRYSTALLIZATION OF THE ENZYME

被引：31

作者：

BOGGARAM, V ^{[1
]}

BROBJER, T ^{[1
]}

LARSON, K ^{[1
]}

MANNERVIK, B ^{[1
]}

机构：

[1] UNIV STOCKHOLM,WENNER GREN INST,DEPT BIOCHEM,S-11345 STOCKHOLM,SWEDEN

来源：

ANALYTICAL BIOCHEMISTRY | 1979年 / 98卷 / 02期

关键词：

D O I：

10.1016/0003-2697(79)90150-7

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Glutathione reductase has been purified to homogeneity from porcine erythrocytes by use of affinity chromatography on 2′,5′-ADP-Sepharose 4B. The enzyme was crystallized from an ammonium sulfate solution. Some of the physical and kinetic properties of the purified enzyme are reported. © 1979.

引用

页码：335 / 340

页数：6

共 9 条

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[8] GLUTATHIONE REDUCTASE FROM HUMAN ERYTHROCYTES - CATALYTIC PROPERTIES AND AGGREGATION [J].

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[9] HUMAN GLUTATHIONE REDUCTASE - PURIFICATION OF CRYSTALLINE ENZYME FROM ERYTHROCYTES [J].

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EUROPEAN JOURNAL OF BIOCHEMISTRY, 1974, 48 (01) :167-177

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